1g3f

Solution NMR

NMR STRUCTURE OF A 9 RESIDUE PEPTIDE FROM SMAC/DIABLO COMPLEXED TO THE BIR3 DOMAIN OF XIAP

Released:

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase XIAP Chain: A
Molecule details ›
Chain: A
Length: 117 amino acids
Theoretical weight: 13.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P98170 (Residues: 241-356; Coverage: 23%)
Gene names: API3, BIRC4, IAP3, XIAP
Sequence domains: Inhibitor of Apoptosis domain
Structure domains: Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A
Diablo homolog, mitochondrial Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 943 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9NR28 (Residues: 56-64; Coverage: 4%)
Gene names: DIABLO, SMAC

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli
  • Not provided